Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode

Wang, Hanyu; Johs, Alexander; Browning, James F.; Tennant, David Alan; Liang, Liyuan

doi:10.1016/j.bioelechem.2019.05.012

Title: Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode

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Abstract

We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°_ET, of 0.4 s^-1 for the native form and 0.55 s^-1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°_ET = 8.0·10^-3 cm·s^-1 at pH 7.07. In conclusion, modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.

Authors:

^[1];

^[1]

Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)

Publication Date:: Thu May 23 00:00:00 EDT 2019

Research Org.:: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)

Sponsoring Org.:: USDOE

OSTI Identifier:: 1530101

Alternate Identifier(s):: OSTI ID: 1703959

Grant/Contract Number:: AC05-00OR22725

Resource Type:: Accepted Manuscript

Journal Name:: Bioelectrochemistry

Additional Journal Information:: Journal Volume: 129; Journal Issue: C; Journal ID: ISSN 1567-5394

Publisher:: Elsevier

Country of Publication:: United States

Language:: English

Subject:: 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Hematite; Cytochrome; Electron transfer; Cyclic voltammetry; Adsorption

Citation Formats


                    Wang, Hanyu, Johs, Alexander, Browning, James F., Tennant, David Alan, and Liang, Liyuan. Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode.  United States: N. p., 2019. 
Web.  doi:10.1016/j.bioelechem.2019.05.012.

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                    Wang, Hanyu, Johs, Alexander, Browning, James F., Tennant, David Alan, & Liang, Liyuan. Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode.  United States.  https://doi.org/10.1016/j.bioelechem.2019.05.012

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                    Wang, Hanyu, Johs, Alexander, Browning, James F., Tennant, David Alan, and Liang, Liyuan. Thu .  
"Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode".  United States.  https://doi.org/10.1016/j.bioelechem.2019.05.012.  https://www.osti.gov/servlets/purl/1530101.

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@article{osti_1530101,

  title        = {Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode},

  author       = {Wang, Hanyu and Johs, Alexander and Browning, James F. and Tennant, David Alan and Liang, Liyuan},

  abstractNote = {We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°ET, of 0.4 s-1 for the native form and 0.55 s-1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°ET = 8.0·10-3 cm·s-1 at pH 7.07. In conclusion, modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.},

  doi          = {10.1016/j.bioelechem.2019.05.012},

  journal      = {Bioelectrochemistry},

  number       = C,

  volume       = 129,

  place        = {United States},

  year         = {Thu May 23 00:00:00 EDT 2019},

  month        = {Thu May 23 00:00:00 EDT 2019}

}

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